Summary for peptidase A01.017: endothiapepsin

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Inhibitors

 

Names
MEROPS Nameendothiapepsin
Other namesEndothia aspartic proteinase, Suparen
Domain architecture
MEROPS Classification
Classification Clan AA >> Subclan (none) >> Family A1 >> Subfamily A >> A01.017
Holotypeendothiapepsin (Cryphonectria parasitica), Uniprot accession P11838 (peptidase unit: 93-418), MERNUM MER0000928
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeAspartic
PeplistIncluded in the Peplist with identifier PL00015
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.23 (Aspartic endopeptidases) >> Peptidase 3.4.23.22
EnzymologyBRENDA database
Proteolytic eventsCutDB database (1 cleavage)
BiotechnologyUsed in cheese making (Awad et al., 1999; Kim et al., 2004).
PhysiologyEndothiapepsin probably has a role in nutrition of the organism, Endothia parasitica, a plant pathogen, so is potentially implicated in plant pathology.
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/kScissile bond-/-/Alt/- (based on 11 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 1 0 1 0 0 0 0 2
Pro 2 0 0 0 0 0 0 1
Ala 0 3 3 0 0 4 5 0
Val 0 1 1 0 1 1 0 0
Leu 0 0 2 1 1 1 2 1
Ile 0 1 0 0 0 0 0 1
Met 0 0 0 0 0 1 0 0
Phe 1 1 0 2 2 0 0 0
Tyr 0 0 0 1 0 1 0 0
Trp 0 0 0 0 0 0 0 0
Ser 0 1 0 1 0 0 0 0
Thr 0 0 0 0 0 0 1 0
Cys 0 0 0 0 0 0 0 0
Asn 0 0 1 1 0 0 0 0
Gln 0 0 0 1 1 0 0 0
Asp 0 0 0 0 0 0 0 0
Glu 2 0 1 0 0 1 0 0
Lys 0 0 0 4 0 0 0 0
Arg 0 1 0 0 0 1 0 0
His 0 1 1 0 1 1 0 0